dbPTM

EYA3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EYA3_HUMAN
UniProt AC	Q99504
Protein Name	Eyes absent homolog 3
Gene Name	EYA3
Organism	Homo sapiens (Human).
Sequence Length	573
Subcellular Localization	Cytoplasm . Nucleus . Localizes at sites of DNA damage at double-strand breaks (DSBs) (PubMed:19234442). With decreasing efficiency, translocalized to the nucleus by SIX2 and SIX5, and SIX4, respectively (By similarity).
Protein Description	Tyrosine phosphatase that specifically dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph). 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Promotes efficient DNA repair by dephosphorylating H2AX, promoting the recruitment of DNA repair complexes containing MDC1. [PubMed: 19234442]
Protein Sequence	MEEEQDLPEQPVKKAKMQESGEQTISQVSNPDVSDQKPETSSLASNLPMSEEIMTCTDYIPRSSNDYTSQMYSAKPYAHILSVPVSETAYPGQTQYQTLQQTQPYAVYPQATQTYGLPPFGALWPGMKPESGLIQTPSPSQHSVLTCTTGLTTSQPSPAHYSYPIQASSTNASLISTSSTIANIPAAAVASISNQDYPTYTILGQNQYQACYPSSSFGVTGQTNSDAESTTLAATTYQSEKPSVMAPAPAAQRLSSGDPSTSPSLSQTTPSKDTDDQSRKNMTSKNRGKRKADATSSQDSELERVFLWDLDETIIIFHSLLTGSYAQKYGKDPTVVIGSGLTMEEMIFEVADTHLFFNDLEECDQVHVEDVASDDNGQDLSNYSFSTDGFSGSGGSGSHGSSVGVQGGVDWMRKLAFRYRKVREIYDKHKSNVGGLLSPQRKEALQRLRAEIEVLTDSWLGTALKSLLLIQSRKNCVNVLITTTQLVPALAKVLLYGLGEIFPIENIYSATKIGKESCFERIVSRFGKKVTYVVIGDGRDEEIAAKQHNMPFWRITNHGDLVSLHQALELDFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEEEQDLP -------CHHCCCCC	15.33	19413330
13	Acetylation	DLPEQPVKKAKMQES CCCCCCCCHHHCHHH	54.41	25953088
37	Sumoylation	NPDVSDQKPETSSLA CCCCCCCCCCCCCHH	50.22	-
59	Phosphorylation	EIMTCTDYIPRSSND CHHHHCCCCCCCCCC	8.48	23879269
63	O-linked_Glycosylation	CTDYIPRSSNDYTSQ HCCCCCCCCCCCCHH	28.30	30059200
63	Phosphorylation	CTDYIPRSSNDYTSQ HCCCCCCCCCCCCHH	28.30	28348404
64	Phosphorylation	TDYIPRSSNDYTSQM CCCCCCCCCCCCHHC	34.69	28348404
67	Phosphorylation	IPRSSNDYTSQMYSA CCCCCCCCCHHCCCC	16.73	27251275
77	Phosphorylation	QMYSAKPYAHILSVP HCCCCCCCEEEEECC	15.31	-
86	O-linked_Glycosylation	HILSVPVSETAYPGQ EEEECCCCCCCCCCC	24.14	30059200
88	O-linked_Glycosylation	LSVPVSETAYPGQTQ EECCCCCCCCCCCCH	24.80	30059200
96	Phosphorylation	AYPGQTQYQTLQQTQ CCCCCCHHHHHHCCC	13.57	-
173	Ubiquitination	QASSTNASLISTSST ECCCCCCEEECCCHH	28.45	24816145
219	Ubiquitination	YPSSSFGVTGQTNSD CCCHHCCCCCCCCCC	5.25	24816145
226	Ubiquitination	VTGQTNSDAESTTLA CCCCCCCCHHHCEEE	57.32	24816145
226	Ubiquitination	VTGQTNSDAESTTLA CCCCCCCCHHHCEEE	57.32	-
228	Ubiquitination	GQTNSDAESTTLAAT CCCCCCHHHCEEEEE	54.32	24816145
235	Phosphorylation	ESTTLAATTYQSEKP HHCEEEEEEECCCCC	22.04	26074081
236	Phosphorylation	STTLAATTYQSEKPS HCEEEEEEECCCCCC	18.16	26074081
237	Phosphorylation	TTLAATTYQSEKPSV CEEEEEEECCCCCCC	12.99	26074081
239	Phosphorylation	LAATTYQSEKPSVMA EEEEEECCCCCCCCC	36.85	26074081
243	Phosphorylation	TYQSEKPSVMAPAPA EECCCCCCCCCCCCH	35.28	26074081
255	Phosphorylation	APAAQRLSSGDPSTS CCHHHHHHCCCCCCC	34.17	25850435
256	Phosphorylation	PAAQRLSSGDPSTSP CHHHHHHCCCCCCCC	52.38	25159151
260	Phosphorylation	RLSSGDPSTSPSLSQ HHHCCCCCCCCCHHC	46.38	29255136
261	Phosphorylation	LSSGDPSTSPSLSQT HHCCCCCCCCCHHCC	50.47	29255136
262	Phosphorylation	SSGDPSTSPSLSQTT HCCCCCCCCCHHCCC	19.48	23401153
264	Phosphorylation	GDPSTSPSLSQTTPS CCCCCCCCHHCCCCC	40.18	29255136
266	Phosphorylation	PSTSPSLSQTTPSKD CCCCCCHHCCCCCCC	29.80	17525332
268	Phosphorylation	TSPSLSQTTPSKDTD CCCCHHCCCCCCCCC	36.98	23401153
269	Phosphorylation	SPSLSQTTPSKDTDD CCCHHCCCCCCCCCH	20.23	30266825
271	Phosphorylation	SLSQTTPSKDTDDQS CHHCCCCCCCCCHHH	40.86	30266825
272	Acetylation	LSQTTPSKDTDDQSR HHCCCCCCCCCHHHH	66.89	26051181
272	Ubiquitination	LSQTTPSKDTDDQSR HHCCCCCCCCCHHHH	66.89	24816145
274	Phosphorylation	QTTPSKDTDDQSRKN CCCCCCCCCHHHHHH	45.25	30266825
274	Ubiquitination	QTTPSKDTDDQSRKN CCCCCCCCCHHHHHH	45.25	24816145
278	Phosphorylation	SKDTDDQSRKNMTSK CCCCCHHHHHHHCCC	52.82	28450419
295	Phosphorylation	GKRKADATSSQDSEL CCCCCCCCCCCCHHH	29.47	30108239
296	Phosphorylation	KRKADATSSQDSELE CCCCCCCCCCCHHHH	27.94	24719451
297	Phosphorylation	RKADATSSQDSELER CCCCCCCCCCHHHHH	33.38	21815630
300	Phosphorylation	DATSSQDSELERVFL CCCCCCCHHHHHEEE	36.12	24719451
377	Ubiquitination	DVASDDNGQDLSNYS CCCCCCCCCCCCCCE	29.40	29967540
384	Ubiquitination	GQDLSNYSFSTDGFS CCCCCCCEEECCCCC	19.57	29967540
430	Ubiquitination	REIYDKHKSNVGGLL HHHHHHHHCCCCCCC	49.84	29967540
430	Methylation	REIYDKHKSNVGGLL HHHHHHHHCCCCCCC	49.84	-
431	Phosphorylation	EIYDKHKSNVGGLLS HHHHHHHCCCCCCCC	36.15	29396449
438	Phosphorylation	SNVGGLLSPQRKEAL CCCCCCCCHHHHHHH	24.83	19664994
462	Ubiquitination	LTDSWLGTALKSLLL HCHHHHHHHHHHHHH	27.01	29967540
469	Ubiquitination	TALKSLLLIQSRKNC HHHHHHHHHHCCCCC	3.98	29967540
472	Phosphorylation	KSLLLIQSRKNCVNV HHHHHHHCCCCCEEE	37.92	14702039
476	Ubiquitination	LIQSRKNCVNVLITT HHHCCCCCEEEEHHH	2.36	29967540
483	Ubiquitination	CVNVLITTTQLVPAL CEEEEHHHHCHHHHH	12.92	29967540
515	Ubiquitination	YSATKIGKESCFERI CCCCCCCHHHHHHHH	50.34	29967540
529	Ubiquitination	IVSRFGKKVTYVVIG HHHHHCCEEEEEEEC	39.94	29967540
546	Ubiquitination	RDEEIAAKQHNMPFW CCHHHHHHHHCCCEE	42.97	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
67	Y	Phosphorylation	Kinase	SRC	P12931	PSP
72	Y	Phosphorylation	Kinase	SRC	P12931	PSP
77	Y	Phosphorylation	Kinase	SRC	P12931	PSP
90	Y	Phosphorylation	Kinase	SRC	P12931	PSP
96	Y	Phosphorylation	Kinase	SRC	P12931	PSP
105	Y	Phosphorylation	Kinase	SRC	P12931	PSP
108	Y	Phosphorylation	Kinase	SRC	P12931	PSP
138	S	Phosphorylation	Kinase	SRC	P12931	PSP
157	S	Phosphorylation	Kinase	SRC	P12931	PSP
208	Y	Phosphorylation	Kinase	SRC	P12931	PSP
225	S	Phosphorylation	Kinase	SRC	P12931	PSP
237	Y	Phosphorylation	Kinase	SRC	P12931	PSP
266	S	Phosphorylation	Kinase	ATM	Q13315	PSP
325	Y	Phosphorylation	Kinase	SRC	P12931	PSP
426	Y	Phosphorylation	Kinase	SRC	P12931	PSP
438	S	Phosphorylation	Kinase	SRC	P12931	PSP
508	Y	Phosphorylation	Kinase	SRC	P12931	PSP
532	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
266	S	Phosphorylation		19234442
Ser-266 phosphorylation is required for localization at sites of DNA damage and directing interaction with H2AX.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EYA3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EYA3_HUMAN	EYA3	physical	27432908
MTMR3_HUMAN	MTMR3	physical	27432908
SOAT1_HUMAN	SOAT1	physical	27432908
PTH2_HUMAN	PTRH2	physical	27432908
MTMR2_HUMAN	MTMR2	physical	27432908
GRPE1_HUMAN	GRPEL1	physical	27432908
FHL2_HUMAN	FHL2	physical	27432908
T126A_HUMAN	TMEM126A	physical	27432908
SEN34_HUMAN	TSEN34	physical	27432908
STIP1_HUMAN	STIP1	physical	27432908
ANFC_HUMAN	NPPC	physical	27432908
TIM21_HUMAN	TIMM21	physical	27432908
CYBP_HUMAN	CACYBP	physical	27432908
NDKA_HUMAN	NME1	physical	27432908
THTPA_HUMAN	THTPA	physical	27432908
TBP_HUMAN	TBP	physical	27432908
DI3L1_HUMAN	DIS3L	physical	27432908
CC28A_HUMAN	CCDC28A	physical	27432908
STX17_HUMAN	STX17	physical	27432908

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EYA3_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Tyrosine dephosphorylation of H2AX modulates apoptosis and survivaldecisions."; Cook P.J., Ju B.G., Telese F., Wang X., Glass C.K., Rosenfeld M.G.; Nature 458:591-596(2009). Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PHOSPHORYLATION ATSER-266, AND MUTAGENESIS OF SER-266 AND ASP-309.	19234442 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY.	17525332 [Abstract]

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